Reviewed, UniProtKB/Swiss-Prot Q5WSX9 (TPMT_LEGPL)

Names and origin

Protein names

Recommended name:
    Thiopurine S-methyltransferase
    EC=2.1.1.67
Alternative name(s):
    Thiopurine methyltransferase

Gene names

Name:	tpm
Ordered Locus Names:	lpl2747

Organism

Legionella pneumophila (strain Lens) [Complete proteome] [HAMAP]

Taxonomic identifier

297245 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	221 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. HAMAP MF_00812
Subcellular location	Cytoplasm By similarity HAMAP MF_00812.
Sequence similarities	Belongs to the methyltransferase superfamily. TPMT family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	thiopurine S-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 221	221	Thiopurine S-methyltransferase HAMAP MF_00812		PRO_0000220123
Sites
	Binding site	12	1	S-adenosyl-L-methionine By similarity
	Binding site	47	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	68	1	S-adenosyl-L-methionine By similarity
	Binding site	125	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5WSX9-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: FB1215EBD4C7D56E	FASTA	221	25,258
	10 20 30 40 50 60 MNKGQYFWNE LWCEGRISFH KKEVNPDLIA YVSSLNIPAK GRVLVPLCGK SVDMLWLVRQ 70 80 90 100 110 120 GYHVVGIELV EKAILQFVQE HQITVRENTI GQAKQYFTDN LNLWVTDIFA LNSALIEPVD 130 140 150 160 170 180 AIYDRAALVA LPKKLRPAYV DICLKWLKPG GSILLKTLQY NQEKVQGPPY SVSPEEIALS 190 200 210 220 YQQCAKIKLL KSQKRIQEPN DHLFNFGISE VNDSVWCIRK G

References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628337 Genomic DNA. Translation: CAH16990.1.
RefSeq	YP_128074.1.
3D structure databases
SMR	Q5WSX9. Positions 6-220.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5WSX9.
Genome annotation databases
GeneID	3115927.
GenomeReviews	Gene locus lpl2747 in contig CR628337_GR.
KEGG	lpf:lpl2747.
NMPDR	fig|297245.3.peg.1545.
Organism-specific databases
LegioList	lpl2747.
CMR	Search...
Phylogenomic databases
eggNOG	COG0500.
HOGENOM	HBG444929.
OMA	GKSLDMC.
Enzyme and pathway databases
BioCyc	LPNE297245:LPL2747-MONOMER.
Family and domain databases
HAMAP	MF_00812. Thiopur_methtran. [Tree]
InterPro	IPR008854. Thiopurine_S-MeTrfase. IPR016822. Thiopurine_S-MeTrfase_sub. [Graphical view]
Pfam	PF05724. TPMT. 1 hit. [Graphical view]
PIRSF	PIRSF023956. Thiopurine_S-methyltransferase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPMT_LEGPL

Accession

Primary (citable) accession number: Q5WSX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	November 23, 2004
Last modified:	January 19, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)